UniProt: F2SG20

Database: UniProt
Entry: F2SG20_TRIRC

LinkDB:  F2SG20_TRIRC 
Original site:  F2SG20_TRIRC

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Ontology (6)   
   GO (6)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (24)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (3)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (34)   

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ID   F2SG20_TRIRC            Unreviewed;      1652 AA.
AC   F2SG20;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN   ORFNames=TERG_02146 {ECO:0000313|EMBL:EGD85876.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD85876.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; GG700649; EGD85876.1; -; Genomic_DNA.
DR   RefSeq; XP_003237425.1; XM_003237377.1.
DR   STRING; 559305.F2SG20; -.
DR   GeneID; 10378803; -.
DR   VEuPathDB; FungiDB:TERG_02146; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   HOGENOM; CLU_001485_20_0_1; -.
DR   InParanoid; F2SG20; -.
DR   OMA; CLAVQVI; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          7..366
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1529..1637
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          36..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1417..1438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1479..1519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          445..483
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        622..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1479..1518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1652 AA;  182732 MW;  4A82D711F6521247 CRC64;
     MEGGGGNIKV VVRVRPFNSR ERDRNAKCIV QMKGAQTVLT PPPGAEEKSR KGGKSSNTGA
     NAAPEGPRVF AFDKSYWSFD RKAPNYAGQD DLFSDLGAPL LDNAFQGYNN CIFAYGQTGS
     GKSYSMMGYG EEAGVIPKIC KEMFQRISAM QVADTNLTST VEVSYLEIYN ERVRDLLNPA
     NKGNLKVREH PSTGPYVEDL AKLVVQSFSE IEHLMDEGNK ARTVAATNMN ETSSRSHAVF
     TLTLTQKRHD KETTMDTEKV SRISLVDLAG SERATSTGAT GARLKEGAEI NRSLSTLGRV
     IAALADLSSG KKKAVVPYRD SVLTWLLKDS LGGNSMTAMI AAISPADINY DETLSTLRYA
     NSAKRIKNHA VVNEDPNARM IRELKEELAQ LRSKLGGGAA AGVPGAAASA TSAGIPQEEY
     PPGTPLEEQM VTIMQADGSV KKVSKAEIVE QLDQSEKLYK DLNQTWEEKL QKTEEIHKER
     EAALEELGIS IEKGFVGLST PKKMPHLVNL SDDPLLAECL VYNIKPGTTT VGNVDATSSA
     CEIRLNGSKI LHKHCTFEHV DNIVTVIPCE GAAVMVNGVR IDSPQRLRSG FRIILGDFHI
     FRFNHPMEAR AERVEQSLLR HSVTTSQLGS NSNTPGRSGP GHDRTISKTG SEIDGDSSRS
     GSPMPSQRGG GSNGREDWFY ARREAANAIL GTDHKISALT DDELDALFDD VQKARAVRKG
     FYENRFLDME EDSDSLSSYP IREKYMSNGT IDNFSLDTAL TMPGTPKQGE YDESNGSPSN
     GNSNGTNEPD TEKGRMEKAL MEAREEFQQQ LQRQKEAFET QIKGIAHLSG HMTEDGPGFS
     FLEPREIEVA RNVLAHWRRR NYVRMVESVL QHASLLKEAQ VMSHIMDKHV FFQFAIIDVG
     QNMGSSYDLV LNGISGDDDM ALDDAKKPCI AVRVIDFKHN VILLWSLDKL ERRVQAMRQM
     HQYIDRPDYI QHFKLENPFS EQCSPTYSLV GDVDVPLTAV FESRVQDFSV EVVSMYTQNV
     IGILRLSLEP SAAQAPSSTL KFNVVMRDLV GFAEREGTDV HAQLFVPGIS EEGGATTTQI
     INGFDENPVQ FESVHSMSLP LHSPRTSTLK VSIFALVSSM HLDKLLSWDE MRDAPEAPPQ
     KRKAPRIAES EYFQEERHDV FAGVQILELA ENGEYLPVDV VQANSLEAGT YQLHQGLQRR
     IVVNLAHSST ESLPWDDVTG LRVGGIRLLD PWGKVPDLDD GKSADVPLKM IQEPMVKDNA
     DGSSNITIIG QWDSSSHGSL LLDRTTADKY KVQITLRWNL ISSRLQEPIV FELDQCLQIL
     GRSSVRPQSM FKQFWSSTRV VHSTSQMFSV AVRPVSAKRA ADLWRMNTQN DYIKGEELLT
     TWSPRKVSLI KDYIAARKRR HRIAEIEAAR AALSDGSLTP LSANGHSTPL QRNTPEHAER
     REQLLRKYLS LWSASKDPTD TILVKGHIEP PLQGAAFAPT ATASTSTDND SVISSANTSS
     QPSTSTSTDR SSSKPRFLAT ITHIPKNPTV LKSGYLYTPD DTYSLWVRRF VELRLPYLHI
     YSVPDGDEIN VINLRNSHVD HDPDFARLLV GSSGNGLSAR GQPNVFAVFG AQNTFLFASR
     TEAQKIEWIL KIDEGYFSGI NSNHGSRGPS RR
//

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